کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9607037 | 44509 | 2005 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Acrylamide-quenching of Rhizomucor miehei lipase
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Steady-state and time-resolved fluorescence-quenching measurements have been performed to study multitryptophan lipase from filamentous fungus Rhizomucor miehei. Using the steady-state acrylamide fluorescence quenching data and the fluorescence-quenching-resolved-spectra (FQRS) method, the total emission spectrum of native (“closed-lid”) lipase has been decomposed into two distinct spectral components accessible to acrylamide. According to FQRS analysis, more quenchable component has a maximum of fluorescence emission at about 352 nm whereas less quenchable component emits at about 332 nm. The redder component participates in about 60-64% of the total lipase fluorescence and may be characterized by the dynamic and static quenching constants equal to K1 = 3.75 Mâ1 and V1 = 1.12 Mâ1, respectively. The bluer component is quenchable via dynamic mechanism with K2 = 1.97 Mâ1. Significant difference in the values of acrylamide bimolecular rate quenching constants estimated for redder and bluer component (i.e., kq = 1.2 Ã 109 Mâ1 sâ1 vs. kq = 4.3 Ã 108 Mâ1 sâ1, respectively), suggests that tryptophan residues in fungal lipase are not uniformly exposed to the solvent.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 80, Issue 1, 1 July 2005, Pages 9-18
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 80, Issue 1, 1 July 2005, Pages 9-18
نویسندگان
Agnieszka Stobiecka,